slr1641 | ATP-dependent chaperone clpB

AS08 344  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: Cyanobacteria

slr1641 | ATP-dependent chaperone clpB in the group Antibodies for Plant/Algal  / Environmental Stress / Heat shock at Agrisera AB (Antibodies for research) (AS08 344)


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Product name, number (Agrisera, Sweden)

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Product Information


recombinant clpB1 protein, derived from Synechocystis PCC 6803 strain slr1641 sequence; protein has an internal translation site. The nomenclature used is reverse of what is mentioned in the cyanobase.

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 100 µl
Reconstitution For reconstitution add 100 µl of sterile water.
Storage Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Tested applications Western blot (WB)
Recommended dilution 1 : 3000 (WB)
Expected | apparent MW

98.1 | 85.4 and 105 | 95 kDa for Synechocystis


Confirmed reactivity Synechocystis PCC 6803, Solanum lycopersicum
Predicted reactivity Cyanobacteria, Francisella sp.
Species of your interest not listed? Contact us
Not reactive in Chlamydomonas reinhardtii

Application examples

Application examples Application example

western blot detection of slr1641 protein

10 μg of total protein from Synechocystis PCC 6803 wild type (+ClpB1) and slr1641 deletion mutant, control (C) and heat shocked samples (HS) was separated on 8% PAA gel and blotted on nitrocellulose membrane . Filters were blocked (1h), incubated with 1: 3000 anti-ClpB1 antibodies (2h) followed by incubation with 1: 2500 secondary anti-rabbit (1h) coupled to HRP and visualization with chemiluminescent detection reagent.

Courtesy of Dr. Elizabeth Vierling, University of Massachusetts, USA

Additional information

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ClpB protein is essential for resistance to high temperature stress. It functions to dissolve inactive protein aggregates that accumulate at high temperatures. Giese and Vierling (2002) Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J Biol Chem; 277(48): 46310-8.

Product citations

Selected references Gonzalez-Esquer and Vermaas (2013). ClpB1 overproduction in Synechocystis sp. strain PCC 6803 increases tolerance to rapid heat shock. Appl Environ Microbiol. 2013 Oct;79(20):6220-7. doi: 10.1128/AEM.01661-13. Epub 2013 Aug 2.

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